Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome

Shyue-Lee Yean, Gerald Wuenschell, John Termini and Ren-Jang Lin ()
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Shyue-Lee Yean: Beckman Research Institute of the City of Hope
Gerald Wuenschell: Beckman Research Institute of the City of Hope
John Termini: Beckman Research Institute of the City of Hope
Ren-Jang Lin: Beckman Research Institute of the City of Hope

Nature, 2000, vol. 408, issue 6814, 881-884

Abstract: Abstract Introns are removed from nuclear messenger RNA precursors through two sequential phospho-transesterification reactions in a dynamic RNA–protein complex called the spliceosome1,2. But whether splicing is catalysed by small nuclear RNAs3,4 in the spliceosome is unresolved. As the spliceosome is a metalloenzyme5,6,7, it is important to determine whether snRNAs coordinate catalytic metals. Here we show that yeast U6 snRNA coordinates a metal ion that is required for the catalytic activity of the spliceosome. With Mg2+, U6 snRNA with a sulphur substitution for the pro-RP or pro-SP non-bridging phosphoryl oxygen of nucleotide U80 reconstitutes a fully assembled yet catalytically inactive spliceosome. Adding a thiophilic ion such as Mn2+ allows the first transesterification reaction to occur in the U6/sU80(SP)- but not the U6/sU80(RP)-reconstituted spliceosome. Mg2+ competitively inhibits the Mn2+-rescued reaction, indicating that the metal-binding site at U6/U80 exists in the wild-type spliceosome and that the site changes its metal requirement for activity in the SP spliceosome. Thus, U6 snRNA contributes to pre-messenger RNA splicing through metal-ion coordination, which is consistent with RNA catalysis by the spliceosome.

Date: 2000
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DOI: 10.1038/35048617

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